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2v1d

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[[Image:2v1d.jpg|left|200px]]<br /><applet load="2v1d" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2v1d.jpg|left|200px]]
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caption="2v1d, resolution 3.10&Aring;" />
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'''STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3 RECOGNITION'''<br />
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{{Structure
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|PDB= 2v1d |SIZE=350|CAPTION= <scene name='initialview01'>2v1d</scene>, resolution 3.10&Aring;
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|SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3 RECOGNITION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2V1D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1D OCA].
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2V1D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1D OCA].
==Reference==
==Reference==
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Structural basis of LSD1-CoREST selectivity in histone H3 recognition., Forneris F, Binda C, Adamo A, Battaglioli E, Mattevi A, J Biol Chem. 2007 Jul 13;282(28):20070-4. Epub 2007 May 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17537733 17537733]
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Structural basis of LSD1-CoREST selectivity in histone H3 recognition., Forneris F, Binda C, Adamo A, Battaglioli E, Mattevi A, J Biol Chem. 2007 Jul 13;282(28):20070-4. Epub 2007 May 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17537733 17537733]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:52:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:42:19 2008''

Revision as of 16:42, 20 March 2008

Image:2v1d.jpg


PDB ID 2v1d

Drag the structure with the mouse to rotate
, resolution 3.10Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3 RECOGNITION


Overview

Histone demethylase LSD1 regulates transcription by demethylating Lys(4) of histone H3. The crystal structure of the enzyme in complex with CoREST and a substrate-like peptide inhibitor highlights an intricate network of interactions and a folded conformation of the bound peptide. The core of the peptide structure is formed by Arg(2), Gln(5), and Ser(10), which are engaged in specific intramolecular H-bonds. Several charged side chains on the surface of the substrate-binding pocket establish electrostatic interactions with the peptide. The three-dimensional structure predicts that methylated Lys(4) binds in a solvent inaccessible position in front of the flavin cofactor. This geometry is fully consistent with the demethylation reaction being catalyzed through a flavin-mediated oxidation of the substrate amino-methyl group. These features dictate the exquisite substrate specificity of LSD1 and provide a structural framework to explain the fine tuning of its catalytic activity and the active role of CoREST in substrate recognition.

About this Structure

2V1D is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of LSD1-CoREST selectivity in histone H3 recognition., Forneris F, Binda C, Adamo A, Battaglioli E, Mattevi A, J Biol Chem. 2007 Jul 13;282(28):20070-4. Epub 2007 May 30. PMID:17537733

Page seeded by OCA on Thu Mar 20 18:42:19 2008

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